Journal articles
α-Helix Unwinding as Force Buffer in Spectrins
Abstract : Spectrins are cytoskeletal proteins located at the inner face of the plasma membrane, making connections between membrane anchors and the actin cortex, and between actin filaments. Spectrins share a common structure forming a bundle of 3 a-helices and play a major role during cell deformation. Here, we used high-speed force spectroscopy and steered molecular dynamics simulations to understand the mechanical stability of spectrin revealing a molecular force buffering function. We find that spectrin acts as a soft spring at short extensions (70-100Å). Under continuous external stretching, its α-helices unwind leading to a viscous mechanical response over larger extensions (100-300Å), represented by a constant-force plateau in force/extension curves. This viscous force buffering emerges from a quasi-equilibrium competition between disruption and reformation of a-helical hydrogen bonds. Our results suggest
Cited literature [42 references]
https://hal-amu.archives-ouvertes.fr/hal-02106340
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Submitted on : Monday, April 22, 2019 - 10:34:23 PM
Last modification on : Tuesday, January 4, 2022 - 5:11:35 AM
Contributor : Felix Rico Connect in order to contact the contributor
Submitted on : Monday, April 22, 2019 - 10:34:23 PM
Last modification on : Tuesday, January 4, 2022 - 5:11:35 AM
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